Crystal structures of highly constrained substrate and hydrolysis products bound to HIV-1 protease. Implications for the catalytic mechanism

Biochemistry

Volumn 47, Issue 12, 2008, Pages 3736-3744

  Tyndall, Joel D A ^a,b   Pattenden, Leonard K ^b,c   Reid, Robert C ^b   Hu, Shu Hong ^b   Alewood, Dianne ^b   Alewood, Paul F ^b   Walsh, Terry ^c   Fairlie, David P ^b   Martin, Jennifer L ^b  

^a UNIVERSITY OF OTAGO   (New Zealand)

^b UNIVERSITY OF QUEENSLAND   (Australia)

^c QUEENSLAND UNIVERSITY OF TECHNOLOGY   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYST ACTIVITY; CONFORMATIONS; CRYSTAL STRUCTURE; HYDROLYSIS; VIRUSES;

HIV-1 PROTEASE; MACROCYCLIC TRIPEPTIDES; MONOCYCLE BINDING;

ENZYME ACTIVITY;

MACROCYCLIC COMPOUND; PEPTIDE; PROTEINASE;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; COMPLEX FORMATION; CRYSTAL STRUCTURE; ENZYME BINDING; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HUMAN IMMUNODEFICIENCY VIRUS 1; HYDROLYSIS; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN STRUCTURE;

BICYCLO COMPOUNDS, HETEROCYCLIC; BINDING, COMPETITIVE; CATALYSIS; HIV PROTEASE; HIV PROTEASE INHIBITORS; HYDROGEN BONDING; MODELS, MOLECULAR; MOLECULAR CONFORMATION;

HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 41149171747     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi7023157     Document Type: Article

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